Faculty Opinions recommendation of Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion.
By Kenneth M Yamada. 2003
165 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/2904bb71a00e81a75337487a334dd26147fb7efa
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In Molecular Biology
Citations in the corpus
- Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells (2003, unknown): “FX are short-lived structures, containing β3integrin (Ballestrem et al., 2001), vinculin (Rottner et al., 1999b), paxillin, α-actinin (Laukaitis et al., 2001) and possibly Arp2/3 (DeMali et al., 2002).”
- Regulation of actin assembly associated with protrusion and adhesion in cell migration. (2008, background): “However, vinculin does not activate Arp2/3 in vitro (50), and the known activators of Arp2/3 (N-WASP, WAVEs, and cortactin) have not been localized at focal complexes.”
- Genetic and cell biological analysis of integrin outside-in signaling. (2009, background): “Vinculin binding appears to be more transient and is not required for cell motility or spreading, but might be necessary for the relocation of Arp2/3 to nascent adhesions (DeMali et al. 2002).”
- Focal adhesion regulation of cell behavior. (2004, background): “Because vinculin mutants defective in Arp2/3 binding inhibit lamellipodial protrusion [133], it is possible that vinculin localization to focal adhesions sequesters it away from Arp2/3, which will inhibit lamellipodial protrusion.”